Recombinant Human Antibody (VRC01) is capable of binding to HIV-1 gp120, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HIV-1 gp120 mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-HIV-1 gp120 mAb and CL of human light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition.
Figure 1 Binding specificity of VRC06 to gp120 defined by ELISA.
(A) VRC06 binding to YU2 gp120 was sensitive to gp120 mutations in both the CD4bs (D368R) and the CoRbs (I420R). Control MAbs included CD4bs ligands (VRC01 and b12) and CoRbs MAb 17b. (B) VRC06 competed with biotin-labeled CD4bs and CoRbs MAb binding to YU2 gp120. (C) sCD4 competed with CD4bs MAbs and enhanced CoRbs MAb binding to gp120. The CD4bs ligands were VRC01, b12, and CD4-Ig; the CoRbs MAbs were 17b, 48d, and 2.1C. The MAb 2G12 was used as negative control.
Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.
Figure 2 Binding of VRC03, VRC06, and VRC06b to JR-FL gp160ΔCT-transfected 293T cell surface by FACS assay, represented by MFI (mean of fluorescence intensity). JR-FL gp160ΔCT is the cleaved trimer; JR-FL gp160ΔCT cleavage-defective is the uncleaved trimer, which contains two mutations that render it cleavage defective.
Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.
Figure 3 VRC06 neutralization potency against JR-FL gp160ΔCT virus was affected by Env mutations leading to an alteration of neutralization sensitivity. Top graphs, Env mutants Δ301 and T569A/I675V display enhanced neutralization sensitivity to CD4bs MAb F105 but substantially decreased neutralization sensitivity to VRC06; the bar graphs on the bottom depict the effects of the Env mutations Δ301 and T569A/I675V on the HIV sensitivity (IC50 values) to VRC06 and other CD4bs ligands.
Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.
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• Increased sensitivity
• Confirmed specificity
• High repeatability
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MRO-029LC-VHH | Anti-HIV-1 gp120 Recombinant Antibody (MRO-029LC-VHH) | ELISA | Single domain antibody |
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(Creative Biolabs Cat# PABL-171, RRID: AB_3111633)
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